HEADER PROTEIN BINDING 09-OCT-24 9H1F TITLE COFILIN-1 IN COMPLEX WITH HIGH-AFFINITY SYBODY B12 COMPND MOL_ID: 1; COMPND 2 MOLECULE: COFILIN-1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: 18 KDA PHOSPHOPROTEIN,P18,COFILIN,NON-MUSCLE ISOFORM; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: SYBODYB12; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CFL1, CFL; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 10 ORGANISM_TAXID: 32630; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS COFILIN-1, CFL1, ADF/COFILIN, G-ACTIN, F-ACTIN, ACTIN, SYBODY, KEYWDS 2 NANOBODY, SYNTHETIC NANOBODY, ACTIN BINDING PROTEIN, ABP, PROTEIN KEYWDS 3 BINDING EXPDTA X-RAY DIFFRACTION AUTHOR T.PARASCHIAKOS,S.WINDHORST,V.POGENBERG REVDAT 1 19-MAR-25 9H1F 0 JRNL AUTH T.PARASCHIAKOS,J.LI,J.SCHOLZ,S.J.HAN,M.DECKERS,V.POGENBERG, JRNL AUTH 2 J.FAIX,S.WINDHORST JRNL TITL A HIGH AFFINITY SYBODY BLOCKS COFILIN-1 BINDING TO F-ACTIN JRNL TITL 2 IN VITRO AND IN CANCER CELLS JRNL REF BIOCHEM.PHARM. 16866 2025 JRNL REFN ISSN 0006-2952 JRNL DOI 10.1016/J.BCP.2025.116866 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.49 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 36817 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.204 REMARK 3 R VALUE (WORKING SET) : 0.203 REMARK 3 FREE R VALUE : 0.226 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.860 REMARK 3 FREE R VALUE TEST SET COUNT : 1789 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 29.4900 - 4.2300 1.00 2914 154 0.1943 0.2124 REMARK 3 2 4.2300 - 3.3600 0.96 2659 136 0.1639 0.1959 REMARK 3 3 3.3600 - 2.9300 1.00 2724 138 0.2021 0.2024 REMARK 3 4 2.9300 - 2.6700 1.00 2718 143 0.2048 0.2536 REMARK 3 5 2.6700 - 2.4800 1.00 2691 127 0.2131 0.2013 REMARK 3 6 2.4700 - 2.3300 1.00 2678 138 0.2140 0.2404 REMARK 3 7 2.3300 - 2.2100 1.00 2697 123 0.2288 0.2873 REMARK 3 8 2.2100 - 2.1200 1.00 2663 139 0.2237 0.2720 REMARK 3 9 2.1200 - 2.0300 1.00 2666 135 0.2233 0.2629 REMARK 3 10 2.0300 - 1.9600 1.00 2672 134 0.2201 0.2286 REMARK 3 11 1.9600 - 1.9000 1.00 2650 148 0.2579 0.2756 REMARK 3 12 1.9000 - 1.8500 1.00 2617 163 0.3362 0.4019 REMARK 3 13 1.8500 - 1.8000 1.00 2679 111 0.4739 0.6009 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.284 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.204 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 38.24 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.10 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.010 2138 REMARK 3 ANGLE : 1.010 2887 REMARK 3 CHIRALITY : 0.065 323 REMARK 3 PLANARITY : 0.008 369 REMARK 3 DIHEDRAL : 12.649 796 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 18 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 67 THROUGH 85 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.7862 14.8773 2.4366 REMARK 3 T TENSOR REMARK 3 T11: 0.2537 T22: 0.1902 REMARK 3 T33: 0.4333 T12: -0.0067 REMARK 3 T13: 0.0111 T23: -0.0156 REMARK 3 L TENSOR REMARK 3 L11: 6.4124 L22: 1.4495 REMARK 3 L33: 7.9347 L12: -2.4394 REMARK 3 L13: -5.6727 L23: 2.0825 REMARK 3 S TENSOR REMARK 3 S11: -0.1138 S12: 0.1849 S13: -0.1061 REMARK 3 S21: 0.0082 S22: -0.0392 S23: -0.0238 REMARK 3 S31: 0.0803 S32: -0.2036 S33: 0.1058 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 86 THROUGH 100 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.8676 14.2281 14.5369 REMARK 3 T TENSOR REMARK 3 T11: 0.2539 T22: 0.2225 REMARK 3 T33: 0.3186 T12: -0.0185 REMARK 3 T13: -0.0050 T23: 0.0076 REMARK 3 L TENSOR REMARK 3 L11: 0.3790 L22: 8.1531 REMARK 3 L33: 3.9082 L12: -0.4936 REMARK 3 L13: 0.6189 L23: 1.3923 REMARK 3 S TENSOR REMARK 3 S11: -0.1071 S12: -0.2654 S13: -0.0954 REMARK 3 S21: 0.5782 S22: 0.2494 S23: -0.3051 REMARK 3 S31: 0.1914 S32: -0.1621 S33: -0.1518 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 101 THROUGH 109 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.1962 3.2729 9.5551 REMARK 3 T TENSOR REMARK 3 T11: 0.3585 T22: 0.2741 REMARK 3 T33: 0.6786 T12: 0.0379 REMARK 3 T13: -0.1035 T23: -0.0347 REMARK 3 L TENSOR REMARK 3 L11: 1.6178 L22: 5.2298 REMARK 3 L33: 0.3362 L12: -0.4677 REMARK 3 L13: -0.1996 L23: 1.1903 REMARK 3 S TENSOR REMARK 3 S11: 0.3208 S12: -0.1196 S13: -0.1490 REMARK 3 S21: 0.7256 S22: 0.1886 S23: -1.9486 REMARK 3 S31: 0.1671 S32: 0.2512 S33: -0.5787 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 110 THROUGH 116 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.6424 20.8537 19.2151 REMARK 3 T TENSOR REMARK 3 T11: 0.3202 T22: 0.2705 REMARK 3 T33: 0.4015 T12: -0.0107 REMARK 3 T13: -0.0067 T23: -0.0384 REMARK 3 L TENSOR REMARK 3 L11: 7.2810 L22: 9.5203 REMARK 3 L33: 9.3531 L12: -2.4271 REMARK 3 L13: -3.9630 L23: 3.3178 REMARK 3 S TENSOR REMARK 3 S11: 0.0711 S12: -0.2269 S13: 0.2864 REMARK 3 S21: 0.7424 S22: 0.0050 S23: 0.2798 REMARK 3 S31: -0.4234 S32: -0.2494 S33: -0.1785 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 12 THROUGH 25 ) REMARK 3 ORIGIN FOR THE GROUP (A): 20.1045 -17.4657 20.9755 REMARK 3 T TENSOR REMARK 3 T11: 0.4468 T22: 0.5201 REMARK 3 T33: 0.5430 T12: 0.0857 REMARK 3 T13: 0.0799 T23: 0.0445 REMARK 3 L TENSOR REMARK 3 L11: 4.5715 L22: 4.3152 REMARK 3 L33: 8.9440 L12: -4.4229 REMARK 3 L13: 1.8638 L23: -1.4661 REMARK 3 S TENSOR REMARK 3 S11: -0.8805 S12: -1.3290 S13: -0.1882 REMARK 3 S21: 1.0834 S22: 0.6710 S23: -0.3334 REMARK 3 S31: 0.6110 S32: -0.5726 S33: 0.0093 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 26 THROUGH 39 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.6343 -33.4595 19.1356 REMARK 3 T TENSOR REMARK 3 T11: 0.3712 T22: 0.4519 REMARK 3 T33: 0.5051 T12: 0.0475 REMARK 3 T13: 0.0657 T23: 0.0927 REMARK 3 L TENSOR REMARK 3 L11: 7.1792 L22: 4.6725 REMARK 3 L33: 2.4264 L12: -5.7463 REMARK 3 L13: 0.3413 L23: -0.7495 REMARK 3 S TENSOR REMARK 3 S11: -0.2317 S12: -0.2845 S13: -0.8973 REMARK 3 S21: 0.6125 S22: 0.6362 S23: 1.3066 REMARK 3 S31: 0.9973 S32: -0.3001 S33: -0.3840 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 40 THROUGH 60 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.2344 -16.2529 11.6733 REMARK 3 T TENSOR REMARK 3 T11: 0.2837 T22: 0.2739 REMARK 3 T33: 0.5877 T12: 0.0118 REMARK 3 T13: 0.0443 T23: 0.0455 REMARK 3 L TENSOR REMARK 3 L11: 2.6567 L22: 5.0404 REMARK 3 L33: 8.2927 L12: -1.8586 REMARK 3 L13: -2.0155 L23: 2.4239 REMARK 3 S TENSOR REMARK 3 S11: 0.0476 S12: 0.1895 S13: -0.4927 REMARK 3 S21: 0.2372 S22: -0.1163 S23: 0.9778 REMARK 3 S31: 0.1777 S32: -0.9037 S33: 0.0102 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 61 THROUGH 87 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.5015 -23.0054 3.9408 REMARK 3 T TENSOR REMARK 3 T11: 0.2637 T22: 0.2091 REMARK 3 T33: 0.4284 T12: -0.0117 REMARK 3 T13: -0.0016 T23: -0.0322 REMARK 3 L TENSOR REMARK 3 L11: 5.3651 L22: 3.3959 REMARK 3 L33: 5.7071 L12: -1.4463 REMARK 3 L13: 1.4459 L23: -2.0441 REMARK 3 S TENSOR REMARK 3 S11: 0.0537 S12: 0.0592 S13: -0.4703 REMARK 3 S21: -0.5756 S22: -0.0437 S23: -0.0757 REMARK 3 S31: 0.6539 S32: 0.2837 S33: -0.0204 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 88 THROUGH 97 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.8178 -17.5735 11.5214 REMARK 3 T TENSOR REMARK 3 T11: 0.2186 T22: 0.1882 REMARK 3 T33: 0.3386 T12: 0.0090 REMARK 3 T13: 0.0168 T23: -0.0279 REMARK 3 L TENSOR REMARK 3 L11: 6.9265 L22: 7.0023 REMARK 3 L33: 4.1392 L12: -4.2672 REMARK 3 L13: 1.4356 L23: -0.7951 REMARK 3 S TENSOR REMARK 3 S11: -0.1819 S12: -0.6100 S13: -0.3259 REMARK 3 S21: 0.2036 S22: 0.3062 S23: -0.3040 REMARK 3 S31: 0.0867 S32: 0.3486 S33: -0.1203 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 98 THROUGH 117 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.1815 -13.1519 9.6063 REMARK 3 T TENSOR REMARK 3 T11: 0.2079 T22: 0.1728 REMARK 3 T33: 0.4430 T12: -0.0223 REMARK 3 T13: -0.0339 T23: -0.0178 REMARK 3 L TENSOR REMARK 3 L11: 4.2658 L22: 4.0123 REMARK 3 L33: 2.8101 L12: -2.9424 REMARK 3 L13: 0.5337 L23: -0.3000 REMARK 3 S TENSOR REMARK 3 S11: -0.2767 S12: -0.2509 S13: -0.0126 REMARK 3 S21: 0.2564 S22: 0.2290 S23: -0.2697 REMARK 3 S31: -0.0830 S32: 0.2927 S33: -0.0110 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 118 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.4297 -4.2847 12.9356 REMARK 3 T TENSOR REMARK 3 T11: 0.4112 T22: 0.1691 REMARK 3 T33: 0.4885 T12: 0.0041 REMARK 3 T13: 0.1052 T23: -0.0330 REMARK 3 L TENSOR REMARK 3 L11: 3.8069 L22: 8.4569 REMARK 3 L33: 8.7766 L12: -1.1612 REMARK 3 L13: 2.1845 L23: -6.6059 REMARK 3 S TENSOR REMARK 3 S11: -0.1353 S12: -0.3155 S13: 0.2066 REMARK 3 S21: 0.9415 S22: -0.0248 S23: 0.3565 REMARK 3 S31: -0.3661 S32: -0.1995 S33: 0.1723 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 135 THROUGH 164 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.0040 -10.8303 7.9242 REMARK 3 T TENSOR REMARK 3 T11: 0.3259 T22: 0.2445 REMARK 3 T33: 0.6667 T12: -0.0037 REMARK 3 T13: 0.0451 T23: -0.0383 REMARK 3 L TENSOR REMARK 3 L11: 8.0634 L22: 4.5608 REMARK 3 L33: 5.1142 L12: -2.5525 REMARK 3 L13: 2.8435 L23: -1.3994 REMARK 3 S TENSOR REMARK 3 S11: -0.1168 S12: 0.1481 S13: 0.5473 REMARK 3 S21: 0.1312 S22: 0.0940 S23: -1.0387 REMARK 3 S31: -0.0241 S32: 0.1259 S33: 0.0146 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 165 THROUGH 173 ) REMARK 3 ORIGIN FOR THE GROUP (A): 43.6102 -20.3962 5.7388 REMARK 3 T TENSOR REMARK 3 T11: 0.3078 T22: 0.2737 REMARK 3 T33: 0.7303 T12: 0.0134 REMARK 3 T13: 0.0713 T23: 0.0099 REMARK 3 L TENSOR REMARK 3 L11: 6.3029 L22: 8.3624 REMARK 3 L33: 8.2831 L12: 4.2125 REMARK 3 L13: -1.7874 L23: 4.1758 REMARK 3 S TENSOR REMARK 3 S11: 0.1193 S12: 0.2119 S13: 1.2511 REMARK 3 S21: -1.0024 S22: 0.0142 S23: -0.3738 REMARK 3 S31: -0.6113 S32: -0.3469 S33: -0.0782 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 9 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.0656 10.5951 5.3506 REMARK 3 T TENSOR REMARK 3 T11: 0.3166 T22: 0.2964 REMARK 3 T33: 0.7028 T12: 0.0344 REMARK 3 T13: 0.0492 T23: -0.0176 REMARK 3 L TENSOR REMARK 3 L11: 3.1035 L22: 3.1809 REMARK 3 L33: 3.2959 L12: -2.9079 REMARK 3 L13: -0.0240 L23: 1.3466 REMARK 3 S TENSOR REMARK 3 S11: 0.1243 S12: 0.0535 S13: 0.3955 REMARK 3 S21: 0.1068 S22: 0.0708 S23: -2.0618 REMARK 3 S31: 0.4437 S32: 0.7944 S33: -0.2813 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 10 THROUGH 19 ) REMARK 3 ORIGIN FOR THE GROUP (A): 19.8371 25.1754 15.8002 REMARK 3 T TENSOR REMARK 3 T11: 0.3763 T22: 0.2378 REMARK 3 T33: 0.4491 T12: 0.0172 REMARK 3 T13: 0.0323 T23: -0.0939 REMARK 3 L TENSOR REMARK 3 L11: 5.6500 L22: 3.0607 REMARK 3 L33: 4.6511 L12: 2.7089 REMARK 3 L13: 0.8952 L23: -2.3876 REMARK 3 S TENSOR REMARK 3 S11: 0.0725 S12: -0.3413 S13: 0.0184 REMARK 3 S21: 0.3626 S22: -0.1617 S23: 0.3533 REMARK 3 S31: -0.7703 S32: -0.6088 S33: 0.0466 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 20 THROUGH 35 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.1630 10.1776 0.7000 REMARK 3 T TENSOR REMARK 3 T11: 0.2826 T22: 0.1801 REMARK 3 T33: 0.4740 T12: 0.0253 REMARK 3 T13: 0.0000 T23: 0.0034 REMARK 3 L TENSOR REMARK 3 L11: 6.6240 L22: 1.1043 REMARK 3 L33: 7.8226 L12: -1.5701 REMARK 3 L13: -4.3381 L23: 2.2154 REMARK 3 S TENSOR REMARK 3 S11: 0.0983 S12: 0.0590 S13: 0.1365 REMARK 3 S21: -0.3822 S22: 0.1050 S23: -0.9152 REMARK 3 S31: 0.1621 S32: 0.3220 S33: -0.2125 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 36 THROUGH 47 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.3844 7.5227 16.3531 REMARK 3 T TENSOR REMARK 3 T11: 0.4197 T22: 0.2934 REMARK 3 T33: 0.4371 T12: -0.0009 REMARK 3 T13: -0.0251 T23: 0.0414 REMARK 3 L TENSOR REMARK 3 L11: 7.7905 L22: 8.8818 REMARK 3 L33: 2.7499 L12: 0.4653 REMARK 3 L13: 0.5350 L23: 4.8374 REMARK 3 S TENSOR REMARK 3 S11: 0.0135 S12: -1.1810 S13: -0.2545 REMARK 3 S21: 1.2701 S22: -0.2524 S23: -0.1359 REMARK 3 S31: 1.0744 S32: 0.0602 S33: 0.2696 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 48 THROUGH 66 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.4183 6.4248 5.0031 REMARK 3 T TENSOR REMARK 3 T11: 0.2579 T22: 0.1794 REMARK 3 T33: 0.4622 T12: -0.0154 REMARK 3 T13: 0.0178 T23: 0.0027 REMARK 3 L TENSOR REMARK 3 L11: 3.5255 L22: 4.1595 REMARK 3 L33: 9.7923 L12: 0.3374 REMARK 3 L13: 1.4602 L23: -0.3519 REMARK 3 S TENSOR REMARK 3 S11: 0.1176 S12: 0.1616 S13: -0.2035 REMARK 3 S21: -0.1264 S22: -0.0518 S23: 0.3350 REMARK 3 S31: 0.5292 S32: -0.2244 S33: -0.0222 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9H1F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-OCT-24. REMARK 100 THE DEPOSITION ID IS D_1292142328. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-JUL-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY REMARK 200 BEAMLINE : P14 (MX2) REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97623 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 S 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JUN 30, 2023 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.15 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36823 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800 REMARK 200 RESOLUTION RANGE LOW (A) : 29.490 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 26.60 REMARK 200 R MERGE (I) : 0.08500 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 21.7900 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.89700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.360 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.8.3 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRIC ACID PH 4.0 AND 2.4 M REMARK 280 AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y+1/2,X+1/2,Z REMARK 290 4555 Y+1/2,-X+1/2,Z REMARK 290 5555 -X+1/2,Y+1/2,-Z REMARK 290 6555 X+1/2,-Y+1/2,-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 60.78750 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 60.78750 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 60.78750 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 60.78750 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 60.78750 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 60.78750 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 60.78750 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 60.78750 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1360 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 13200 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 SER A 1 REMARK 465 ASN A 2 REMARK 465 ILE A 3 REMARK 465 GLY A 4 REMARK 465 SER A 5 REMARK 465 GLY A 6 REMARK 465 SER A 7 REMARK 465 MET A 8 REMARK 465 ALA A 9 REMARK 465 SER A 10 REMARK 465 GLY A 11 REMARK 465 VAL A 27 REMARK 465 ARG A 28 REMARK 465 LYS A 29 REMARK 465 SER A 30 REMARK 465 SER A 31 REMARK 465 GLY B 1 REMARK 465 HIS B 2 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A 26 CD CE NZ REMARK 470 GLU A 49 CG CD OE1 OE2 REMARK 470 LYS A 99 CG CD CE NZ REMARK 470 GLU A 100 CG CD OE1 OE2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 HIS B 56 -84.81 61.04 REMARK 500 REMARK 500 REMARK: NULL DBREF 9H1F A 8 173 UNP P23528 COF1_HUMAN 1 166 DBREF 9H1F B 1 116 PDB 9H1F 9H1F 1 116 SEQADV 9H1F SER A 1 UNP P23528 EXPRESSION TAG SEQADV 9H1F ASN A 2 UNP P23528 EXPRESSION TAG SEQADV 9H1F ILE A 3 UNP P23528 EXPRESSION TAG SEQADV 9H1F GLY A 4 UNP P23528 EXPRESSION TAG SEQADV 9H1F SER A 5 UNP P23528 EXPRESSION TAG SEQADV 9H1F GLY A 6 UNP P23528 EXPRESSION TAG SEQADV 9H1F SER A 7 UNP P23528 EXPRESSION TAG SEQRES 1 A 173 SER ASN ILE GLY SER GLY SER MET ALA SER GLY VAL ALA SEQRES 2 A 173 VAL SER ASP GLY VAL ILE LYS VAL PHE ASN ASP MET LYS SEQRES 3 A 173 VAL ARG LYS SER SER THR PRO GLU GLU VAL LYS LYS ARG SEQRES 4 A 173 LYS LYS ALA VAL LEU PHE CYS LEU SER GLU ASP LYS LYS SEQRES 5 A 173 ASN ILE ILE LEU GLU GLU GLY LYS GLU ILE LEU VAL GLY SEQRES 6 A 173 ASP VAL GLY GLN THR VAL ASP ASP PRO TYR ALA THR PHE SEQRES 7 A 173 VAL LYS MET LEU PRO ASP LYS ASP CYS ARG TYR ALA LEU SEQRES 8 A 173 TYR ASP ALA THR TYR GLU THR LYS GLU SER LYS LYS GLU SEQRES 9 A 173 ASP LEU VAL PHE ILE PHE TRP ALA PRO GLU SER ALA PRO SEQRES 10 A 173 LEU LYS SER LYS MET ILE TYR ALA SER SER LYS ASP ALA SEQRES 11 A 173 ILE LYS LYS LYS LEU THR GLY ILE LYS HIS GLU LEU GLN SEQRES 12 A 173 ALA ASN CYS TYR GLU GLU VAL LYS ASP ARG CYS THR LEU SEQRES 13 A 173 ALA GLU LYS LEU GLY GLY SER ALA VAL ILE SER LEU GLU SEQRES 14 A 173 GLY LYS PRO LEU SEQRES 1 B 116 GLY HIS GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 B 116 VAL GLN ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 B 116 SER GLY PHE PRO VAL ASN HIS ARG THR MET ALA TRP TYR SEQRES 4 B 116 ARG GLN ALA PRO GLY LYS GLU ARG GLU TRP VAL ALA ALA SEQRES 5 B 116 ILE GLU SER HIS GLY GLN GLU THR TRP TYR ALA ASP SER SEQRES 6 B 116 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 B 116 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 B 116 ASP THR ALA VAL TYR TYR CYS VAL ARG VAL GLY ALA GLU SEQRES 9 B 116 TYR VAL GLY GLN GLY THR GLN VAL THR VAL SER ALA FORMUL 3 HOH *183(H2 O) HELIX 1 AA1 SER A 15 LYS A 26 1 12 HELIX 2 AA2 PRO A 33 LYS A 38 1 6 HELIX 3 AA3 GLY A 65 VAL A 67 5 3 HELIX 4 AA4 ASP A 73 LEU A 82 1 10 HELIX 5 AA5 PRO A 117 LEU A 135 1 19 HELIX 6 AA6 CYS A 146 LYS A 151 1 6 HELIX 7 AA7 ASP A 152 GLY A 162 1 11 HELIX 8 AA8 SER A 163 VAL A 165 5 3 HELIX 9 AA9 PRO B 30 ARG B 34 5 5 HELIX 10 AB1 LYS B 89 THR B 93 5 5 SHEET 1 AA1 6 ALA A 13 VAL A 14 0 SHEET 2 AA1 6 ASN A 53 LEU A 63 1 O ILE A 54 N ALA A 13 SHEET 3 AA1 6 LYS A 40 LEU A 47 -1 N LYS A 41 O ILE A 62 SHEET 4 AA1 6 ARG A 88 GLU A 97 -1 O TYR A 89 N PHE A 45 SHEET 5 AA1 6 LYS A 102 TRP A 111 -1 O LYS A 103 N TYR A 96 SHEET 6 AA1 6 GLU A 141 ALA A 144 1 O LEU A 142 N PHE A 108 SHEET 1 AA2 6 ALA A 13 VAL A 14 0 SHEET 2 AA2 6 ASN A 53 LEU A 63 1 O ILE A 54 N ALA A 13 SHEET 3 AA2 6 LYS A 40 LEU A 47 -1 N LYS A 41 O ILE A 62 SHEET 4 AA2 6 ARG A 88 GLU A 97 -1 O TYR A 89 N PHE A 45 SHEET 5 AA2 6 SER A 167 LEU A 168 -1 O SER A 167 N GLU A 97 SHEET 6 AA2 6 LYS A 171 PRO A 172 -1 O LYS A 171 N LEU A 168 SHEET 1 AA3 4 GLN B 5 SER B 9 0 SHEET 2 AA3 4 LEU B 20 SER B 27 -1 O ALA B 25 N VAL B 7 SHEET 3 AA3 4 THR B 80 MET B 85 -1 O MET B 85 N LEU B 20 SHEET 4 AA3 4 PHE B 70 ASP B 75 -1 N THR B 71 O GLN B 84 SHEET 1 AA4 6 GLY B 12 GLN B 15 0 SHEET 2 AA4 6 THR B 110 SER B 115 1 O THR B 113 N VAL B 14 SHEET 3 AA4 6 ALA B 94 ARG B 100 -1 N TYR B 96 O THR B 110 SHEET 4 AA4 6 MET B 36 GLN B 41 -1 N TYR B 39 O TYR B 97 SHEET 5 AA4 6 GLU B 48 ILE B 53 -1 O ALA B 51 N TRP B 38 SHEET 6 AA4 6 THR B 60 TYR B 62 -1 O TRP B 61 N ALA B 52 CRYST1 121.575 121.575 52.346 90.00 90.00 90.00 P 4 21 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.008225 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008225 0.000000 0.00000 SCALE3 0.000000 0.000000 0.019104 0.00000